7XBF
The complex structure of RshSTT182/200 RBD-insert2 bound to human ACE2
Summary for 7XBF
Entry DOI | 10.2210/pdb7xbf/pdb |
Descriptor | Processed angiotensin-converting enzyme 2, RshSTT182/200 coronavirus receptor binding domain insert2, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | complex, viral protein |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 4 |
Total formula weight | 195767.91 |
Authors | |
Primary citation | Hu, Y.,Liu, K.,Han, P.,Xu, Z.,Zheng, A.,Pan, X.,Jia, Y.,Su, C.,Tang, L.,Wu, L.,Bai, B.,Zhao, X.,Tian, D.,Chen, Z.,Qi, J.,Wang, Q.,Gao, G.F. Host range and structural analysis of bat-origin RshSTT182/200 coronavirus binding to human ACE2 and its animal orthologs. Embo J., 42:e111737-e111737, 2023 Cited by PubMed Abstract: Bat-origin RshSTT182 and RshSTT200 coronaviruses (CoV) from Rhinolophus shameli in Southeast Asia (Cambodia) share 92.6% whole-genome identity with SARS-CoV-2 and show identical receptor-binding domains (RBDs). In this study, we determined the structure of the RshSTT182/200 receptor binding domain (RBD) in complex with human angiotensin-converting enzyme 2 (hACE2) and identified the key residues that influence receptor binding. The binding of the RshSTT182/200 RBD to ACE2 orthologs from 39 animal species, including 18 bat species, was used to evaluate its host range. The RshSTT182/200 RBD broadly recognized 21 of 39 ACE2 orthologs, although its binding affinities for the orthologs were weaker than those of the RBD of SARS-CoV-2. Furthermore, RshSTT182 pseudovirus could utilize human, fox, and Rhinolophus affinis ACE2 receptors for cell entry. Moreover, we found that SARS-CoV-2 induces cross-neutralizing antibodies against RshSTT182 pseudovirus. Taken together, these findings indicate that RshSTT182/200 can potentially infect susceptible animals, but requires further evolution to obtain strong interspecies transmission abilities like SARS-CoV-2. PubMed: 36519268DOI: 10.15252/embj.2022111737 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.51 Å) |
Structure validation
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